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Database: PDB
Entry: 5VAY
LinkDB: 5VAY
Original site: 5VAY 
HEADER    APOPTOSIS                               28-MAR-17   5VAY              
TITLE     BCL-2 COMPLEX WITH BECLIN 1 T108D BH3 DOMAIN                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: APOPTOSIS REGULATOR BCL-2 -- BCL-2-LIKE PROTEIN 1 CHIMERA; 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: BCL2-L-1,APOPTOSIS REGULATOR BCL-X;                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: BECLIN-1;                                                  
COMPND   8 CHAIN: E, G, F, H;                                                   
COMPND   9 SYNONYM: COILED-COIL MYOSIN-LIKE BCL2-INTERACTING PROTEIN,PROTEIN    
COMPND  10 GT197;                                                               
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: BCL2, BCL2L1, BCL2L, BCLX;                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606                                                 
KEYWDS    APOPTOSIS, BCL-2, AUTOPHAGY, BECLIN 1                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.F.LEE,B.J.SMITH,S.YAO,W.D.FAIRLIE                                   
REVDAT   1   04-APR-18 5VAY    0                                                
JRNL        AUTH   E.F.LEE,B.J.SMITH,S.YAO,W.D.FAIRLIE                          
JRNL        TITL   BCL-2 COMPLEX WITH BECLIN 1 PT108 BH3 DOMAIN                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 71180                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3559                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 44.4510 -  5.2722    0.98     2803   147  0.1836 0.2272        
REMARK   3     2  5.2722 -  4.1857    1.00     2784   147  0.1463 0.1870        
REMARK   3     3  4.1857 -  3.6569    0.99     2739   144  0.1584 0.1892        
REMARK   3     4  3.6569 -  3.3227    0.99     2696   142  0.1615 0.2112        
REMARK   3     5  3.3227 -  3.0846    0.99     2754   145  0.1815 0.2590        
REMARK   3     6  3.0846 -  2.9027    0.99     2720   143  0.1905 0.1950        
REMARK   3     7  2.9027 -  2.7574    0.99     2707   142  0.1792 0.1958        
REMARK   3     8  2.7574 -  2.6374    0.99     2705   143  0.1819 0.2558        
REMARK   3     9  2.6374 -  2.5359    0.99     2713   143  0.1909 0.2152        
REMARK   3    10  2.5359 -  2.4484    0.99     2697   141  0.1841 0.2120        
REMARK   3    11  2.4484 -  2.3718    0.99     2731   144  0.1878 0.2561        
REMARK   3    12  2.3718 -  2.3040    0.99     2671   141  0.1882 0.2512        
REMARK   3    13  2.3040 -  2.2434    0.99     2706   142  0.1865 0.2724        
REMARK   3    14  2.2434 -  2.1886    0.99     2685   142  0.1901 0.2378        
REMARK   3    15  2.1886 -  2.1389    0.99     2705   142  0.1943 0.2444        
REMARK   3    16  2.1389 -  2.0934    0.99     2704   142  0.2067 0.2402        
REMARK   3    17  2.0934 -  2.0515    0.99     2685   142  0.2093 0.2818        
REMARK   3    18  2.0515 -  2.0128    0.99     2704   142  0.2107 0.2261        
REMARK   3    19  2.0128 -  1.9768    0.99     2653   139  0.2105 0.2686        
REMARK   3    20  1.9768 -  1.9433    0.99     2724   144  0.2168 0.2769        
REMARK   3    21  1.9433 -  1.9120    0.99     2684   141  0.2282 0.2821        
REMARK   3    22  1.9120 -  1.8826    0.99     2681   141  0.2364 0.2603        
REMARK   3    23  1.8826 -  1.8549    0.99     2660   140  0.2433 0.3130        
REMARK   3    24  1.8549 -  1.8287    0.99     2712   143  0.2590 0.2999        
REMARK   3    25  1.8287 -  1.8040    0.95     2598   137  0.2948 0.3165        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.360           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           5659                                  
REMARK   3   ANGLE     :  0.979           7680                                  
REMARK   3   CHIRALITY :  0.041            792                                  
REMARK   3   PLANARITY :  0.005           1008                                  
REMARK   3   DIHEDRAL  : 13.304           2030                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  78.0455   8.1132  22.4968              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2010 T22:   0.1578                                     
REMARK   3      T33:   0.2179 T12:  -0.0042                                     
REMARK   3      T13:   0.0183 T23:   0.0064                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3118 L22:   0.0349                                     
REMARK   3      L33:   0.2898 L12:   0.0440                                     
REMARK   3      L13:   0.1203 L23:   0.0919                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0179 S12:   0.0878 S13:   0.0053                       
REMARK   3      S21:  -0.0121 S22:   0.0007 S23:  -0.0118                       
REMARK   3      S31:  -0.0065 S32:   0.0215 S33:   0.0154                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5VAY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAY-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000227145.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-JUL-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 71186                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.4100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2XA0                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS, PH 6.5, 0.2M AMMONIUM         
REMARK 280  ACETATE, 25% PEG 3350, VAPOR DIFFUSION, SITTING DROP,               
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       26.59600            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8510 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8810 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7900 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2000 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7970 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    74                                                      
REMARK 465     ASP A    75                                                      
REMARK 465     ASP A    76                                                      
REMARK 465     VAL A    77                                                      
REMARK 465     GLU A    78                                                      
REMARK 465     GLU A    79                                                      
REMARK 465     ASN A    80                                                      
REMARK 465     ARG A    81                                                      
REMARK 465     THR A    82                                                      
REMARK 465     GLU A    83                                                      
REMARK 465     ALA A    84                                                      
REMARK 465     PRO A    85                                                      
REMARK 465     GLU A    86                                                      
REMARK 465     GLY A    87                                                      
REMARK 465     THR A    88                                                      
REMARK 465     GLU A    89                                                      
REMARK 465     ARG A   207                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     ALA B    73                                                      
REMARK 465     GLY B    74                                                      
REMARK 465     ASP B    75                                                      
REMARK 465     ASP B    76                                                      
REMARK 465     VAL B    77                                                      
REMARK 465     GLU B    78                                                      
REMARK 465     GLU B    79                                                      
REMARK 465     ASN B    80                                                      
REMARK 465     ARG B    81                                                      
REMARK 465     THR B    82                                                      
REMARK 465     GLU B    83                                                      
REMARK 465     ALA B    84                                                      
REMARK 465     PRO B    85                                                      
REMARK 465     GLU B    86                                                      
REMARK 465     GLY B    87                                                      
REMARK 465     THR B    88                                                      
REMARK 465     MET B   206                                                      
REMARK 465     ARG B   207                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     HIS C     3                                                      
REMARK 465     ALA C     4                                                      
REMARK 465     GLY C     5                                                      
REMARK 465     ARG C     6                                                      
REMARK 465     THR C     7                                                      
REMARK 465     GLY C     8                                                      
REMARK 465     GLY C    74                                                      
REMARK 465     ASP C    75                                                      
REMARK 465     ASP C    76                                                      
REMARK 465     VAL C    77                                                      
REMARK 465     GLU C    78                                                      
REMARK 465     GLU C    79                                                      
REMARK 465     ASN C    80                                                      
REMARK 465     ARG C    81                                                      
REMARK 465     THR C    82                                                      
REMARK 465     GLU C    83                                                      
REMARK 465     ALA C    84                                                      
REMARK 465     PRO C    85                                                      
REMARK 465     GLU C    86                                                      
REMARK 465     GLY C    87                                                      
REMARK 465     THR C    88                                                      
REMARK 465     GLU C    89                                                      
REMARK 465     SER C   205                                                      
REMARK 465     MET C   206                                                      
REMARK 465     ARG C   207                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     SER D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     HIS D     3                                                      
REMARK 465     ALA D     4                                                      
REMARK 465     GLY D     5                                                      
REMARK 465     ARG D     6                                                      
REMARK 465     THR D     7                                                      
REMARK 465     GLY D     8                                                      
REMARK 465     TYR D     9                                                      
REMARK 465     ALA D    73                                                      
REMARK 465     GLY D    74                                                      
REMARK 465     ASP D    75                                                      
REMARK 465     ASP D    76                                                      
REMARK 465     VAL D    77                                                      
REMARK 465     GLU D    78                                                      
REMARK 465     GLU D    79                                                      
REMARK 465     ASN D    80                                                      
REMARK 465     ARG D    81                                                      
REMARK 465     THR D    82                                                      
REMARK 465     GLU D    83                                                      
REMARK 465     ALA D    84                                                      
REMARK 465     PRO D    85                                                      
REMARK 465     GLU D    86                                                      
REMARK 465     GLY D    87                                                      
REMARK 465     THR D    88                                                      
REMARK 465     GLU D    89                                                      
REMARK 465     PRO D   204                                                      
REMARK 465     SER D   205                                                      
REMARK 465     MET D   206                                                      
REMARK 465     ARG D   207                                                      
REMARK 465     ASP E   105                                                      
REMARK 465     GLY E   106                                                      
REMARK 465     GLY E   107                                                      
REMARK 465     GLN E   129                                                      
REMARK 465     THR E   130                                                      
REMARK 465     ASP G   105                                                      
REMARK 465     GLY G   106                                                      
REMARK 465     GLY G   128                                                      
REMARK 465     GLN G   129                                                      
REMARK 465     THR G   130                                                      
REMARK 465     ASP F   105                                                      
REMARK 465     GLY F   106                                                      
REMARK 465     GLY F   107                                                      
REMARK 465     GLN F   129                                                      
REMARK 465     THR F   130                                                      
REMARK 465     ASP H   105                                                      
REMARK 465     GLY H   106                                                      
REMARK 465     GLY H   107                                                      
REMARK 465     GLY H   128                                                      
REMARK 465     GLN H   129                                                      
REMARK 465     THR H   130                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ALA A 113    CB                                                  
REMARK 470     GLN A 118    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 164    CD   NE   CZ   NH1  NH2                             
REMARK 470     SER A 205    OG                                                  
REMARK 470     MET A 206    CG   SD   CE                                        
REMARK 470     ASP B  31    CB   CG   OD1  OD2                                  
REMARK 470     GLU B 114    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 118    CG   CD   OE1  NE2                                  
REMARK 470     HIS B 120    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU B 175    CG   CD1  CD2                                       
REMARK 470     ARG C  26    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP C  31    CB   CG   OD1  OD2                                  
REMARK 470     ARG C 110    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 114    CG   CD   OE1  OE2                                  
REMARK 470     ASP D  31    CB   CG   OD1  OD2                                  
REMARK 470     ARG D 109    CD   NE                                             
REMARK 470     ARG D 110    NE   CZ   NH1  NH2                                  
REMARK 470     GLN D 118    CG   CD   OE1  NE2                                  
REMARK 470     ARG D 129    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 183    NE   CZ   NH1  NH2                                  
REMARK 470     ASP E 108    CG   OD1  OD2                                       
REMARK 470     GLU E 110    CG   CD   OE1  OE2                                  
REMARK 470     ARG E 114    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU G 110    CG   CD   OE1  OE2                                  
REMARK 470     ARG G 114    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU F 110    CG   CD   OE1  OE2                                  
REMARK 470     GLU H 110    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   394     O    HOH A   395              1.78            
REMARK 500   OG   SER C   105     OE1  GLU C   152              2.11            
REMARK 500   OH   TYR A    28     OD1  ASN A   163              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE1  GLN A    25     O    HOH A   395     2746     1.85            
REMARK 500   OD1  ASP B   191     O    HOH B   346     2856     2.15            
REMARK 500   O    HOH D   323     O    HOH D   332     2645     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA B 113      171.11     54.86                                   
REMARK 500    GLU B 114      -83.62     48.53                                   
REMARK 500    MET B 115       64.93     60.47                                   
REMARK 500    ASP C  31      -82.18   -117.34                                   
REMARK 500    ALA C 113     -163.50    -65.40                                   
REMARK 500    ALA D 113     -176.12    -62.96                                   
REMARK 500    ARG D 164       30.78    -99.01                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU B  114     MET B  115                 -149.30                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 394        DISTANCE =  5.82 ANGSTROMS                       
REMARK 525    HOH A 395        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH A 396        DISTANCE =  6.02 ANGSTROMS                       
REMARK 525    HOH A 397        DISTANCE =  7.53 ANGSTROMS                       
REMARK 525    HOH A 398        DISTANCE =  9.20 ANGSTROMS                       
REMARK 525    HOH D 336        DISTANCE =  9.26 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5VAX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VAU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VB1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VB4   RELATED DB: PDB                                   
DBREF  5VAY A    1    75  UNP    P10415   BCL2_HUMAN       1     34             
DBREF  5VAY A   76    91  UNP    Q07817   B2CL1_HUMAN     29     44             
DBREF  5VAY A   92   207  UNP    P10415   BCL2_HUMAN      92    207             
DBREF  5VAY B    1    75  UNP    P10415   BCL2_HUMAN       1     34             
DBREF  5VAY B   76    91  UNP    Q07817   B2CL1_HUMAN     29     44             
DBREF  5VAY B   92   207  UNP    P10415   BCL2_HUMAN      92    207             
DBREF  5VAY C    1    75  UNP    P10415   BCL2_HUMAN       1     34             
DBREF  5VAY C   76    91  UNP    Q07817   B2CL1_HUMAN     29     44             
DBREF  5VAY C   92   207  UNP    P10415   BCL2_HUMAN      92    207             
DBREF  5VAY D    1    75  UNP    P10415   BCL2_HUMAN       1     34             
DBREF  5VAY D   76    91  UNP    Q07817   B2CL1_HUMAN     29     44             
DBREF  5VAY D   92   207  UNP    P10415   BCL2_HUMAN      92    207             
DBREF  5VAY E  105   130  UNP    Q14457   BECN1_HUMAN    105    130             
DBREF  5VAY G  105   130  UNP    Q14457   BECN1_HUMAN    105    130             
DBREF  5VAY F  105   130  UNP    Q14457   BECN1_HUMAN    105    130             
DBREF  5VAY H  105   130  UNP    Q14457   BECN1_HUMAN    105    130             
SEQADV 5VAY GLY A   -1  UNP  P10415              EXPRESSION TAG                 
SEQADV 5VAY SER A    0  UNP  P10415              EXPRESSION TAG                 
SEQADV 5VAY GLY B   -1  UNP  P10415              EXPRESSION TAG                 
SEQADV 5VAY SER B    0  UNP  P10415              EXPRESSION TAG                 
SEQADV 5VAY GLY C   -1  UNP  P10415              EXPRESSION TAG                 
SEQADV 5VAY SER C    0  UNP  P10415              EXPRESSION TAG                 
SEQADV 5VAY GLY D   -1  UNP  P10415              EXPRESSION TAG                 
SEQADV 5VAY SER D    0  UNP  P10415              EXPRESSION TAG                 
SEQADV 5VAY ASP E  108  UNP  Q14457    THR   108 ENGINEERED MUTATION            
SEQADV 5VAY ASP G  108  UNP  Q14457    THR   108 ENGINEERED MUTATION            
SEQADV 5VAY ASP F  108  UNP  Q14457    THR   108 ENGINEERED MUTATION            
SEQADV 5VAY ASP H  108  UNP  Q14457    THR   108 ENGINEERED MUTATION            
SEQRES   1 A  168  GLY SER MET ALA HIS ALA GLY ARG THR GLY TYR ASP ASN          
SEQRES   2 A  168  ARG GLU ILE VAL MET LYS TYR ILE HIS TYR LYS LEU SER          
SEQRES   3 A  168  GLN ARG GLY TYR GLU TRP ASP ALA GLY ASP ASP VAL GLU          
SEQRES   4 A  168  GLU ASN ARG THR GLU ALA PRO GLU GLY THR GLU SER GLU          
SEQRES   5 A  168  VAL VAL HIS LEU THR LEU ARG GLN ALA GLY ASP ASP PHE          
SEQRES   6 A  168  SER ARG ARG TYR ARG ARG ASP PHE ALA GLU MET SER SER          
SEQRES   7 A  168  GLN LEU HIS LEU THR PRO PHE THR ALA ARG GLY ARG PHE          
SEQRES   8 A  168  ALA THR VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL ASN          
SEQRES   9 A  168  TRP GLY ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY VAL          
SEQRES  10 A  168  MET CYS VAL GLU SER VAL ASN ARG GLU MET SER PRO LEU          
SEQRES  11 A  168  VAL ASP ASN ILE ALA LEU TRP MET THR GLU TYR LEU ASN          
SEQRES  12 A  168  ARG HIS LEU HIS THR TRP ILE GLN ASP ASN GLY GLY TRP          
SEQRES  13 A  168  ASP ALA PHE VAL GLU LEU TYR GLY PRO SER MET ARG              
SEQRES   1 B  168  GLY SER MET ALA HIS ALA GLY ARG THR GLY TYR ASP ASN          
SEQRES   2 B  168  ARG GLU ILE VAL MET LYS TYR ILE HIS TYR LYS LEU SER          
SEQRES   3 B  168  GLN ARG GLY TYR GLU TRP ASP ALA GLY ASP ASP VAL GLU          
SEQRES   4 B  168  GLU ASN ARG THR GLU ALA PRO GLU GLY THR GLU SER GLU          
SEQRES   5 B  168  VAL VAL HIS LEU THR LEU ARG GLN ALA GLY ASP ASP PHE          
SEQRES   6 B  168  SER ARG ARG TYR ARG ARG ASP PHE ALA GLU MET SER SER          
SEQRES   7 B  168  GLN LEU HIS LEU THR PRO PHE THR ALA ARG GLY ARG PHE          
SEQRES   8 B  168  ALA THR VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL ASN          
SEQRES   9 B  168  TRP GLY ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY VAL          
SEQRES  10 B  168  MET CYS VAL GLU SER VAL ASN ARG GLU MET SER PRO LEU          
SEQRES  11 B  168  VAL ASP ASN ILE ALA LEU TRP MET THR GLU TYR LEU ASN          
SEQRES  12 B  168  ARG HIS LEU HIS THR TRP ILE GLN ASP ASN GLY GLY TRP          
SEQRES  13 B  168  ASP ALA PHE VAL GLU LEU TYR GLY PRO SER MET ARG              
SEQRES   1 C  168  GLY SER MET ALA HIS ALA GLY ARG THR GLY TYR ASP ASN          
SEQRES   2 C  168  ARG GLU ILE VAL MET LYS TYR ILE HIS TYR LYS LEU SER          
SEQRES   3 C  168  GLN ARG GLY TYR GLU TRP ASP ALA GLY ASP ASP VAL GLU          
SEQRES   4 C  168  GLU ASN ARG THR GLU ALA PRO GLU GLY THR GLU SER GLU          
SEQRES   5 C  168  VAL VAL HIS LEU THR LEU ARG GLN ALA GLY ASP ASP PHE          
SEQRES   6 C  168  SER ARG ARG TYR ARG ARG ASP PHE ALA GLU MET SER SER          
SEQRES   7 C  168  GLN LEU HIS LEU THR PRO PHE THR ALA ARG GLY ARG PHE          
SEQRES   8 C  168  ALA THR VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL ASN          
SEQRES   9 C  168  TRP GLY ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY VAL          
SEQRES  10 C  168  MET CYS VAL GLU SER VAL ASN ARG GLU MET SER PRO LEU          
SEQRES  11 C  168  VAL ASP ASN ILE ALA LEU TRP MET THR GLU TYR LEU ASN          
SEQRES  12 C  168  ARG HIS LEU HIS THR TRP ILE GLN ASP ASN GLY GLY TRP          
SEQRES  13 C  168  ASP ALA PHE VAL GLU LEU TYR GLY PRO SER MET ARG              
SEQRES   1 D  168  GLY SER MET ALA HIS ALA GLY ARG THR GLY TYR ASP ASN          
SEQRES   2 D  168  ARG GLU ILE VAL MET LYS TYR ILE HIS TYR LYS LEU SER          
SEQRES   3 D  168  GLN ARG GLY TYR GLU TRP ASP ALA GLY ASP ASP VAL GLU          
SEQRES   4 D  168  GLU ASN ARG THR GLU ALA PRO GLU GLY THR GLU SER GLU          
SEQRES   5 D  168  VAL VAL HIS LEU THR LEU ARG GLN ALA GLY ASP ASP PHE          
SEQRES   6 D  168  SER ARG ARG TYR ARG ARG ASP PHE ALA GLU MET SER SER          
SEQRES   7 D  168  GLN LEU HIS LEU THR PRO PHE THR ALA ARG GLY ARG PHE          
SEQRES   8 D  168  ALA THR VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL ASN          
SEQRES   9 D  168  TRP GLY ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY VAL          
SEQRES  10 D  168  MET CYS VAL GLU SER VAL ASN ARG GLU MET SER PRO LEU          
SEQRES  11 D  168  VAL ASP ASN ILE ALA LEU TRP MET THR GLU TYR LEU ASN          
SEQRES  12 D  168  ARG HIS LEU HIS THR TRP ILE GLN ASP ASN GLY GLY TRP          
SEQRES  13 D  168  ASP ALA PHE VAL GLU LEU TYR GLY PRO SER MET ARG              
SEQRES   1 E   26  ASP GLY GLY ASP MET GLU ASN LEU SER ARG ARG LEU LYS          
SEQRES   2 E   26  VAL THR GLY ASP LEU PHE ASP ILE MET SER GLY GLN THR          
SEQRES   1 G   26  ASP GLY GLY ASP MET GLU ASN LEU SER ARG ARG LEU LYS          
SEQRES   2 G   26  VAL THR GLY ASP LEU PHE ASP ILE MET SER GLY GLN THR          
SEQRES   1 F   26  ASP GLY GLY ASP MET GLU ASN LEU SER ARG ARG LEU LYS          
SEQRES   2 F   26  VAL THR GLY ASP LEU PHE ASP ILE MET SER GLY GLN THR          
SEQRES   1 H   26  ASP GLY GLY ASP MET GLU ASN LEU SER ARG ARG LEU LYS          
SEQRES   2 H   26  VAL THR GLY ASP LEU PHE ASP ILE MET SER GLY GLN THR          
FORMUL   9  HOH   *256(H2 O)                                                    
HELIX    1 AA1 THR A    7  GLN A   25  1                                  19    
HELIX    2 AA2 GLU A   91  PHE A  112  1                                  22    
HELIX    3 AA3 GLU A  114  LEU A  119  5                                   6    
HELIX    4 AA4 THR A  125  PHE A  138  1                                  14    
HELIX    5 AA5 ASN A  143  ARG A  164  1                                  22    
HELIX    6 AA6 PRO A  168  LEU A  185  1                                  18    
HELIX    7 AA7 LEU A  185  ASN A  192  1                                   8    
HELIX    8 AA8 GLY A  193  GLY A  203  1                                  11    
HELIX    9 AA9 ARG B    6  GLN B   25  1                                  20    
HELIX   10 AB1 SER B   90  ALA B  113  1                                  24    
HELIX   11 AB2 THR B  122  PHE B  138  1                                  17    
HELIX   12 AB3 ASN B  143  ARG B  164  1                                  22    
HELIX   13 AB4 PRO B  168  LEU B  185  1                                  18    
HELIX   14 AB5 LEU B  185  ASN B  192  1                                   8    
HELIX   15 AB6 GLY B  193  GLY B  203  1                                  11    
HELIX   16 AB7 ASP C   10  GLN C   25  1                                  16    
HELIX   17 AB8 GLU C   91  PHE C  112  1                                  22    
HELIX   18 AB9 GLU C  114  LEU C  119  5                                   6    
HELIX   19 AC1 THR C  125  ARG C  139  1                                  15    
HELIX   20 AC2 ASN C  143  ARG C  164  1                                  22    
HELIX   21 AC3 PRO C  168  LEU C  185  1                                  18    
HELIX   22 AC4 LEU C  185  ASN C  192  1                                   8    
HELIX   23 AC5 GLY C  193  GLY C  203  1                                  11    
HELIX   24 AC6 ASN D   11  GLN D   25  1                                  15    
HELIX   25 AC7 GLU D   91  PHE D  112  1                                  22    
HELIX   26 AC8 GLU D  114  LEU D  119  5                                   6    
HELIX   27 AC9 THR D  125  ARG D  139  1                                  15    
HELIX   28 AD1 ASN D  143  ARG D  164  1                                  22    
HELIX   29 AD2 PRO D  168  LEU D  185  1                                  18    
HELIX   30 AD3 LEU D  185  ASN D  192  1                                   8    
HELIX   31 AD4 GLY D  193  GLY D  203  1                                  11    
HELIX   32 AD5 MET E  109  GLY E  128  1                                  20    
HELIX   33 AD6 ASP G  108  SER G  127  1                                  20    
HELIX   34 AD7 MET F  109  GLY F  128  1                                  20    
HELIX   35 AD8 MET H  109  MET H  126  1                                  18    
CRYST1   85.205   53.192   91.413  90.00 108.39  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011736  0.000000  0.003903        0.00000                         
SCALE2      0.000000  0.018800  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011528        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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